Q8VQF6
Gene name |
cinA |
Protein name |
1,8-cineole 2-endo-monooxygenase |
Names |
cytochrome P450, CYP176A1, P450cin |
Species |
Citrobacter braakii |
KEGG Pathway |
ag:AAL57614 |
EC number |
1.14.14.133: With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
10 structures for Q8VQF6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1T2B | X-ray | 170 A | A/B | 8-404 | PDB |
| 3BDZ | X-ray | 200 A | A/B | 8-404 | PDB |
| 3BE0 | X-ray | 305 A | A/B | 8-404 | PDB |
| 4FB2 | X-ray | 137 A | A/B/C/D | 8-404 | PDB |
| 4FMX | X-ray | 155 A | A/B | 8-404 | PDB |
| 4FYZ | X-ray | 232 A | A/B | 8-404 | PDB |
| 4L6G | X-ray | 137 A | A/B | 8-404 | PDB |
| 4L77 | X-ray | 138 A | A/B | 8-404 | PDB |
| 4LHT | X-ray | 214 A | A/B | 8-404 | PDB |
| AF-Q8VQF6-F1 | Predicted | AlphaFoldDB |
No variants for Q8VQF6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8VQF6 | |||||
No associated diseases with Q8VQF6
No regional properties for Q8VQF6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8VQF6 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.14.133 | With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| iron ion binding | Binding to an iron (Fe) ion. |
| oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| carbazole catabolic process | The chemical reactions and pathways resulting in the breakdown of carbazole, a heterocyclic aromatic compound containing a dibenzopyrrole system that is produced during coal gasification and is present in cigarette smoke. Coal tar produced at high temperature contains an average of 1.5% carbazole. It is used widely in synthesis of dyes, pharmaceuticals, and plastics and is a suspected carcinogen. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTATVASTSL | FTTADHYHTP | LGPDGTPHAF | FEALRDEAET | TPIGWSEAYG | GHWVVAGYKE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IQAVIQNTKA | FSNKGVTFPR | YETGEFELMM | AGQDDPVHKK | YRQLVAKPFS | PEATDLFTEQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LRQSTNDLID | ARIELGEGDA | ATWLANEIPA | RLTAILLGLP | PEDGDTYRRW | VWAITHVENP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EEGAEIFAEL | VAHARTLIAE | RRTNPGNDIM | SRVIMSKIDG | ESLSEDDLIG | FFTILLLGGI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DNTARFLSSV | FWRLAWDIEL | RRRLIAHPEL | IPNAVDELLR | FYGPAMVGRL | VTQEVTVGDI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TMKPGQTAML | WFPIASRDRS | AFDSPDNIVI | ERTPNRHLSL | GHGIHRCLGA | HLIRVEARVA |
| 370 | 380 | 390 | 400 | ||
| ITEFLKRIPE | FSLDPNKECE | WLMGQVAGML | HVPIIFPKGK | RLSE |